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β-淀粉样蛋白诱导血小板聚集并促进血小板黏附。

beta-Amyloid protein induces platelet aggregation and supports platelet adhesion.

作者信息

Kowalska M A, Badellino K

机构信息

Department of Physiology, Temple University School of Medicine, Philadelphia, Pa. 19140.

出版信息

Biochem Biophys Res Commun. 1994 Dec 30;205(3):1829-35. doi: 10.1006/bbrc.1994.2883.

DOI:10.1006/bbrc.1994.2883
PMID:7811271
Abstract

The amyloid precursor protein (APP) is found in many cells including neurons, endothelial cells and blood platelets. Beta-amyloid protein (beta AP) is derived from APP and is deposited in brain and in cerebral microvasculature of individuals with Alzheimer's disease. In this study we demonstrate that beta AP interacts with human blood platelets. We found that human beta AP peptide (1-40) fibrils aggregate platelets and support their adhesion, and these interactions are mediated through platelet membrane integrin receptors.

摘要

淀粉样前体蛋白(APP)存在于包括神经元、内皮细胞和血小板在内的许多细胞中。β-淀粉样蛋白(β-AP)由APP衍生而来,沉积在阿尔茨海默病患者的大脑和脑微血管中。在本研究中,我们证明β-AP与人类血小板相互作用。我们发现人类β-AP肽(1-40)纤维聚集血小板并支持其黏附,并且这些相互作用是通过血小板膜整合素受体介导的。

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beta-Amyloid protein induces platelet aggregation and supports platelet adhesion.β-淀粉样蛋白诱导血小板聚集并促进血小板黏附。
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Beta-amyloid augments platelet aggregation: reduced activity of familial angiopathy-associated mutants.β-淀粉样蛋白增强血小板聚集:家族性血管病相关突变体活性降低。
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Thrombospondin binding to specific sequences within the A alpha- and B beta-chains of fibrinogen.血小板反应蛋白与纤维蛋白原Aα链和Bβ链内的特定序列结合。
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